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Retromer in Alzheimer disease, Parkinson disease and other neurological disorders

Small, Scott A., Petsko, Gregory A.·2015·Nature Reviews Neuroscience
DOI 10.1038/nrn3896
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Abstract

Retromer is a protein assembly that has a central role in endosomal trafficking, and retromer dysfunction has been linked to a growing number of neurological disorders. First linked to Alzheimer disease, retromer dysfunction causes a range of pathophysiological consequences that have been shown to contribute to the core pathological features of the disease. Genetic studies have established that retromer dysfunction is also pathogenically linked to Parkinson disease, although the biological mechanisms that mediate this link are only now being elucidated. Most recently, studies have shown that retromer is a tractable target in drug discovery for these and other disorders of the nervous system.

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  • Retromer core proteins are deficient in the hippocampal formation of patients with Alzheimer's disease.

    “Retromer core proteins are deficient in the hippocampal formation of patients with AD, and depleting VPS35, the core’s central protein, has emerged as the most reliable approach for disrupting retromer-dependent endosomal recycling (Small and Petsko, 2015).”

    From The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease (2022) · cites this paper as Small and Petsko, 2015

  • SORL1 can act as a retromer-receptor that allows the retromer coat to interact with APP and GluA1 cargo.

    “based on older (Small and Petsko, 2015) and newer studies (Mishra et al., 2021), SORL1 (sortilin-related receptor1) can act a retromer-receptor that allows the retromer coat to interact with this cargo.”

    From The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease (2022) · cites this paper as Small and Petsko, 2015

  • Depleting VPS35 is the most reliable approach for disrupting retromer-dependent endosomal recycling.

    “Retromer core proteins are deficient in the hippocampal formation of patients with AD, and depleting VPS35, the core’s central protein, has emerged as the most reliable approach for disrupting retromer-dependent endosomal recycling (Small and Petsko, 2015).”

    From The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease (2022) · cites this paper as Small and Petsko, 2015

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Research works printed but not linked: 79

  1. Schekman, R. Charting the secretory pathway in a simple eukaryote. Mol. Biol. Cell 21, 3781–3784 (2010). · DOI
  2. Henne, W. M., Buchkovich, N. J. & Emr, S. D. The ESCRT pathway. Dev. Cell 21, 77–91 (2011). · DOI
  3. Seaman, M. N., McCaffery, J. M. & Emr, S. D. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665–681 (1998). · DOI · Paper page
  4. Haft, C. R. et al. Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. Mol. Biol. Cell 11, 4105–4116 (2000). · DOI · Paper page
  5. Seaman, M. N. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111–122 (2004). · DOI · Paper page
  6. Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R. & Bonifacino, J. S. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123–133 (2004). · DOI · Paper page
  7. Small, S. A. et al. Model-guided microarray implicates the retromer complex in Alzheimer's disease. Ann. Neurol. 58, 909–919 (2005). · DOI · Paper page
  8. Carroll, R. C., Beattie, E. C., von Zastrow, M. & Malenka, R. C. Role of AMPA receptor endocytosis in synaptic plasticity. Nature Rev. Neurosci. 2, 315–324 (2001). · DOI · Paper page
  9. Choy, R. W. et al. Retromer mediates a discrete route of local membrane delivery to dendrites. Neuron 82, 55–62 (2014). · DOI · Paper page
  10. Zhang, D. et al. RAB-6.2 and the retromer regulate glutamate receptor recycling through a retrograde pathway. J. Cell Biol. 196, 85–101 (2012). · DOI · Paper page
  11. Hussain, N. K., Diering, G. H., Sole, J., Anggono, V. & Huganir, R. L. Sorting nexin 27 regulates basal and activity-dependent trafficking of AMPARs. Proc. Natl Acad. Sci. USA 111, 11840–11845 (2014). · DOI · Paper page
  12. Loo, L. S., Tang, N., Al-Haddawi, M., Dawe, G. S. & Hong, W. A role for sorting nexin 27 in AMPA receptor trafficking. Nature Commun. 5, 3176 (2014). · DOI · Paper page
  13. Feinstein, T. N. et al. Retromer terminates the generation of cAMP by internalized PTH receptors. Nature Chem. Biol. 7, 278–284 (2011). · DOI
  14. Temkin, P. et al. SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nature Cell Biol. 13, 715–721 (2011). · DOI · Paper page
  15. Seaman, M. N. Recycle your receptors with retromer. Trends Cell Biol. 15, 68–75 (2005). · DOI · Paper page
  16. Kerr, M. C. et al. A novel mammalian retromer component, Vps26B. Traffic 6, 991–1001 (2005). · DOI · Paper page
  17. Collins, B. M. et al. Structure of Vps26B and mapping of its interaction with the retromer protein complex. Traffic 9, 366–379 (2008). · DOI
  18. Kim, E. et al. Identification of novel retromer complexes in the mouse testis. Biochem. Biophys. Res. Commun. 375, 16–21 (2008). · DOI
  19. Bugarcic, A. et al. Vps26A and Vps26B subunits define distinct retromer complexes. Traffic 12, 1759–1773 (2011). · DOI
  20. Gallon, M. et al. A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27–retromer. Proc. Natl Acad. Sci. USA 111, E3604–E3613 (2014). · DOI · Paper page
  21. Kim, E. et al. Implication of mouse Vps26b–Vps29–Vps35 retromer complex in sortilin trafficking. Biochem. Biophys. Res. Commun. 403, 167–171 (2010). · DOI
  22. Attar, N. & Cullen, P. J. The retromer complex. Adv. Enzyme Regul. 50, 216–236 (2010). · DOI
  23. Rojas, R., Kametaka, S., Haft, C. R. & Bonifacino, J. S. Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. Mol. Cell. Biol. 27, 1112–1124 (2007). · DOI
  24. Wassmer, T. et al. A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45–54 (2007). · DOI · Paper page
  25. Sierecki, E. et al. Rapid mapping of interactions between human SNX–BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy. Mol. Cell. Proteom. 13, 2233–2245 (2014). · DOI
  26. van Weering, J. R. et al. Molecular basis for SNX–BAR-mediated assembly of distinct endosomal sorting tubules. EMBO J. 31, 4466–4480 (2012). · DOI · Paper page
  27. Harbour, M. E. et al. The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics. J. Cell Sci. 123, 3703–3717 (2010). · DOI · Paper page
  28. Harterink, M. et al. A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion. Nature Cell Biol. 13, 914–923 (2011). · DOI · Paper page
  29. Rojas, R. et al. Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7. J. Cell Biol. 183, 513–526 (2008). · DOI · Paper page
  30. Seaman, M. N., Harbour, M. E., Tattersall, D., Read, E. & Bright, N. Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab–GAP TBC1D5. J. Cell Sci. 122, 2371–2382 (2009). · DOI · Paper page
  31. Harrison, M. S. et al. A mechanism for retromer endosomal coat complex assembly with cargo. Proc. Natl Acad. Sci. USA 111, 267–272 (2014). · DOI
  32. Cozier, G. E. et al. The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation. J. Biol. Chem. 277, 48730–48736 (2002). · DOI · Paper page
  33. Steinberg, F. et al. A global analysis of SNX27–retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nature Cell Biol. 15, 461–471 (2013). · DOI · Paper page
  34. Derivery, E. & Gautreau, A. Evolutionary conservation of the WASH complex, an actin polymerization machine involved in endosomal fission. Commun. Integr. Biol. 3, 227–230 (2010). · DOI
  35. Gomez, T. S. & Billadeau, D. D. A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev. Cell 17, 699–711 (2009). · DOI · Paper page
  36. Rogaeva, E. et al. The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease. Nature Genet. 39, 168–177 (2007). · DOI · Paper page
  37. Bhalla, A. et al. The location and trafficking routes of the neuronal retromer and its role in amyloid precursor protein transport. Neurobiol. Dis. 47, 126–134 (2012). · DOI · Paper page
  38. Fjorback, A. W. et al. Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing. J. Neurosci. 32, 1467–1480 (2012). · DOI · Paper page
  39. Lane, R. F. et al. Vps10 family proteins and the retromer complex in aging-related neurodegeneration and diabetes. J. Neurosci. 32, 14080–14086 (2012). · DOI
  40. Small, S. A. & Gandy, S. Sorting through the cell biology of Alzheimer's disease: intracellular pathways to pathogenesis. Neuron 52, 15–31 (2006). · DOI
  41. Canuel, M., Korkidakis, A., Konnyu, K. & Morales, C. R. Sortilin mediates the lysosomal targeting of cathepsins D and H. Biochem. Biophys. Res. Commun. 373, 292–297 (2008). · DOI
  42. Futerman, A. H. & van Meer, G. The cell biology of lysosomal storage disorders. Nature Rev. Mol. Cell Biol. 5, 554–565 (2004). · DOI
  43. Zavodszky, E. et al. Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy. Nature Commun. 5, 3828 (2014). · DOI · Paper page
  44. Nixon, R. A. The role of autophagy in neurodegenerative disease. Nature Med. 19, 983–997 (2013). · DOI · Paper page
  45. Dhungel, R. et al. Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron 85, 76–87 (2015). · DOI
  46. Walker, L. C., Diamond, M. I., Duff, K. E. & Hyman, B. T. Mechanisms of protein seeding in neurodegenerative diseases. JAMA Neurol. 70, 304–310 (2013). · DOI · Paper page
  47. Luk, K. C. et al. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949–953 (2012). · DOI · Paper page
  48. Small, S. A. Isolating pathogenic mechanisms embedded within the hippocampal circuit through regional vulnerability. Neuron 84, 32–39 (2014). · DOI
  49. Moreno, H. et al. Imaging the Aβ-related neurotoxicity of Alzheimer disease. Arch. Neurol. 64, 1467–1477 (2007). · DOI
  50. Dodson, S. E. et al. LR11/SorLA expression is reduced in sporadic Alzheimer disease but not in familial Alzheimer disease. J. Neuropathol. Exp. Neurol. 65, 866–872 (2006). · DOI · Paper page
  51. Vardarajan, B. N. et al. Identification of Alzheimer disease-associated variants in genes that regulate retromer function. Neurobiol. Aging 33, 2231.e15–2231.e30 (2012). · DOI · Paper page
  52. Reitz, C. et al. Independent and epistatic effects of variants in VPS10-d receptors on Alzheimer disease risk and processing of the amyloid precursor protein (APP). Transl Psychiatry 3, e256 (2013). · DOI
  53. Lane, R. F. et al. Diabetes-associated SorCS1 regulates Alzheimer's amyloid-β metabolism: evidence for involvement of SorL1 and the retromer complex. J. Neurosci. 30, 13110–13115 (2010). · DOI · Paper page
  54. Vieira, S. I. et al. Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated. Mol. Neurodegener. 5, 40 (2010). · DOI
  55. Mecozzi, V. J. et al. Pharmacological chaperones stabilize retromer to limit APP processing. Nature Chem. Biol. 10, 443–449 (2014). · DOI · Paper page
  56. Choy, R. W., Cheng, Z. & Schekman, R. Amyloid precursor protein (APP) traffics from the cell surface via endosomes for amyloid β (Aβ) production in the trans-Golgi network. Proc. Natl Acad. Sci. USA 109, E2077–E2082 (2012). · DOI
  57. Wu, J. W. et al. Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J. Biol. Chem. 288, 1856–1870 (2013). · DOI · Paper page
  58. Khurana, V. et al. Lysosomal dysfunction promotes cleavage and neurotoxicity of tau in vivo. PLoS Genet. 6, e1001026 (2010). · DOI
  59. Zimprich, A. et al. A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease. Am. J. Hum. Genet. 89, 168–175 (2011). · DOI · Paper page
  60. Vilarino-Guell, C. et al. VPS35 mutations in Parkinson disease. Am. J. Hum. Genet. 89, 162–167 (2011). · DOI · Paper page
  61. Macleod, D. A. et al. RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk. Neuron 77, 425–439 (2013). · DOI · Paper page
  62. Bi, F., Li, F., Huang, C. & Zhou, H. Pathogenic mutation in VPS35 impairs its protection against MPP+ cytotoxicity. Int. J. Biol. Sci. 9, 149–155 (2013). · DOI
  63. Follett, J. et al. The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer. Traffic 15, 230–244 (2014). · DOI
  64. Linhart, R. et al. Vacuolar protein sorting 35 (Vps35) rescues locomotor deficits and shortened lifespan in Drosophila expressing a Parkinson's disease mutant of leucine-rich repeat kinase 2 (LRRK2). Mol. Neurodegener. 9, 23 (2014). · DOI
  65. McGough, I. J. et al. Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation. Curr. Biol. 24, 1670–1676 (2014). · DOI · Paper page
  66. Miura, E. et al. VPS35 dysfunction impairs lysosomal degradation of α-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease. Neurobiol. Dis. 71, 1–13 (2014). · DOI
  67. Tsika, E. et al. Parkinson's disease-linked mutations in VPS35 induce dopaminergic neurodegeneration. Hum. Mol. Genet. 23, 4621–4638 (2014). · DOI · Paper page
  68. Dodson, M. W., Leung, L. K., Lone, M., Lizzio, M. A. & Guo, M. Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo. Dis. Model. Mech. 7, 1351–1363 (2014).
  69. Wang, X. et al. Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome. Nature Med. 19, 473–480 (2013). · DOI · Paper page
  70. Blackstone, C., O'Kane, C. J. & Reid, E. Hereditary spastic paraplegias: membrane traffic and the motor pathway. Nature Rev. Neurosci. 12, 31–42 (2011). · DOI
  71. Valdmanis, P. N. et al. Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary spastic paraplegia. Am. J. Hum. Genet. 80, 152–161 (2007). · DOI · Paper page
  72. Jalanko, A. & Braulke, T. Neuronal ceroid lipofuscinoses. Biochim. Biophys. Acta 1793, 697–709 (2009). · DOI
  73. Metcalf, D. J., Calvi, A. A., Seaman, M., Mitchison, H. M. & Cutler, D. F. Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor. Traffic 9, 1905–1914 (2008). · DOI
  74. Mamo, A., Jules, F., Dumaresq-Doiron, K., Costantino, S. & Lefrancois, S. The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting. Mol. Cell. Biol. 32, 1855–1866 (2012). · DOI · Paper page
  75. Verges, M., Sebastian, I. & Mostov, K. E. Phosphoinositide 3-kinase regulates the role of retromer in transcytosis of the polymeric immunoglobulin receptor. Exp. Cell Res. 313, 707–718 (2007). · DOI
  76. Garber, K. Neurodegeneration. Potential Alzheimer's drug spurs protein recycling. Science 344, 351 (2014). · DOI
  77. Cataldo, A. et al. Endocytic disturbances distinguish among subtypes of Alzheimer's disease and related disorders. Ann. Neurol. 50, 661–665 (2001). · DOI · Paper page
  78. Ye, S. et al. Apolipoprotein (apo) E4 enhances amyloid β peptide production in cultured neuronal cells: apoE structure as a potential therapeutic target. Proc. Natl Acad. Sci. USA 102, 18700–18705 (2005). · DOI · Paper page
  79. Small, S. A. Pharmacological chaperones in the age of proteomic pathology. Proc. Natl Acad. Sci. USA 111, 12274–12275 (2014). · DOI

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Authors
Small, S. A., & Petsko, G. A.
Venue
Nature Reviews Neuroscience
Publisher
Springer Science and Business Media LLC
Published
2015-02-11
Volume
16
Issue
3
Pages
126-132
ISSN
  • 1471-003X
  • 1471-0048
DOI
10.1038/nrn3896
Cited by
227
References
14
Language
en
Update notices
erratum (2015-02-20)
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